4.7 Article

CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites

Journal

JOURNAL OF CELL BIOLOGY
Volume 183, Issue 7, Pages 1223-1233

Publisher

ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200809190

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Funding

  1. Deutsche Forschungsgemeinschaft
  2. European Union
  3. Swiss National Science Foundation ( SNSF)
  4. Centre National de la Recherche Scientifique
  5. Association de la Recherche contre le Cancer [3140]
  6. French National Research Agency ( ANR) [JC05_42022]

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The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells. Several microtubule-associated proteins link microtubules to subcellular structures. A subclass of these proteins, the plus end-binding proteins (+TIPs), selectively binds to the growing plus ends of microtubules. Here, we reconstitute a vertebrate plus end tracking system composed of the most prominent +TIPs, end-binding protein 1 (EB1) and CLIP-170, in vitro and dissect their end-tracking mechanism. We. find that EB1 autonomously recognizes specific binding sites present at growing microtubule ends. In contrast, CLIP-170 does not end-track by itself but requires EB1. CLIP-170 recognizes and turns over rapidly on composite binding sites constituted by end-accumulated EB1 and tyrosinated alpha-tubulin. In contrast to its. fission yeast orthologue Tip1, dynamic end tracking of CLIP-170 does not require the activity of a molecular motor. Our results demonstrate evolutionary diversity of the plus end recognition mechanism of CLIP-170 family members, whereas the autonomous end-tracking mechanism of EB family members is conserved.

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